ArticleProtein science : a publication of the Protein Society2025
A pipeline for screening small molecule-enhanced protein stability in a bacterial orphan receptor.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.bioRxiv : the preprint server for biology · 2026Article
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4 authors.
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Abstract
Bacterial one-component signaling proteins integrate sensory and gene regulation functions within the same polypeptide, creating powerful natural sensors of environmental conditions which can also be adapted into powerful tools for synthetic biology and biotechnology. A key sensor motif within many of these proteins is the Per-ARNT-Sim (PAS) domain, known for its conserved fold yet highly divergent sequences, allowing for a broad range of ligands to control PAS protein function by changes in small molecule binding occupancy or configuration. This diversity introduces a challenging step-identification of ligands for "orphan" PAS proteins which show signatures of ligand binding but no copurifying high-affinity bound small molecules-into characterization and engineering of such proteins. In this study, we characterized CU228, a putative PAS-HTH transcription factor from Candidatus Solibacter usitatus, as a novel model system for searching for novel ligands by small molecule stabilization. Bioinformatics and structural analyses predicted a PAS domain with a Trp-rich internal cavity, suggesting potential small molecule interactions. Using a ~760 compound fragment library, differential scanning fluorimetry identified three ligands (KG-96, KG-408, and KG-484) that substantially increased CU228 thermal stability with ΔT
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